Abstract
During HIV-1 morphogenesis, the precursor Gag protein is processed to release capsid (CA) proteins that form the mature virus core. In this process, the CA proteins assemble a lattice in which N-terminal domain (NTD) helices 1-3 are critical for multimer formation. Mature core assembly requires refolding of the N-terminus of CA into a β-hairpin, but the precise contribution of the hairpin core morphogenesis is unclear. We found that mutations at isoleucine 15 (I15), between the β-hairpin and NTD helix 1 are incompatible with proper mature core assembly. However, a compensatory mutation of histidine 12 in the β-hairpin to a tyrosine was selected by long term passage of an I15 mutant virus in T cells. The tyrosine does not interact directly with residue 15, but with NTD helix 3, supporting a model in which β-hairpin folding serves to align helix 3 for mature NTD multimerization.
Original language | English (US) |
---|---|
Pages (from-to) | 95-103 |
Number of pages | 9 |
Journal | Virology |
Volume | 447 |
Issue number | 1-2 |
DOIs | |
State | Published - Dec 2013 |
Keywords
- Capsid
- Gag
- HIV
- N-terminal domain
- Virus assembly
ASJC Scopus subject areas
- Virology